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121305-26-8

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121305-26-8 Usage

Uses

H-Leu-Pro-Pro-Oh is used in genetic profiling to identify subclonal mutational architecture of human primary and metastatic colorectal cancer.

Check Digit Verification of cas no

The CAS Registry Mumber 121305-26-8 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,2,1,3,0 and 5 respectively; the second part has 2 digits, 2 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 121305-26:
(8*1)+(7*2)+(6*1)+(5*3)+(4*0)+(3*5)+(2*2)+(1*6)=68
68 % 10 = 8
So 121305-26-8 is a valid CAS Registry Number.
InChI:InChI=1/C16H27N3O4/c1-10(2)9-11(17)14(20)18-7-3-5-12(18)15(21)19-8-4-6-13(19)16(22)23/h10-13H,3-9,17H2,1-2H3,(H,22,23)/t11-,12-,13-/m0/s1

121305-26-8SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 20, 2017

Revision Date: Aug 20, 2017

1.Identification

1.1 GHS Product identifier

Product name (2S)-1-[(2S)-1-[(2S)-2-amino-4-methylpentanoyl]pyrrolidine-2-carbonyl]pyrrolidine-2-carboxylic acid

1.2 Other means of identification

Product number -
Other names 1-(1-L-Leucyl-L-prolyl)-L-proline

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:121305-26-8 SDS

121305-26-8Upstream product

121305-26-8Downstream Products

121305-26-8Relevant articles and documents

Characterisation of the hydrolytic specificity of Aspergillus niger derived prolyl endoproteinase on bovine β-casein and determination of ACE inhibitory activity

Norris, Roseanne,Poyarkov, Alexey,O'Keeffe, Martina B.,Fitzgerald, Richard J.

, p. 29 - 36 (2014/03/21)

The hydrolytic specificity of Aspergillus niger prolyl endoproteinase (An-PEP) on purified β-casein (β-CN) was assessed. This analysis confirmed cleavage at the C-terminal side of Pro residues. An-PEP also had the ability to cleave at the C-terminal side of Ala, Glu, Gly, Ser, Lys and Leu. Incubation of purified β-CN with An-PEP resulted in the generation of highly potent angiotensin converting enzyme (ACE) inhibitory hydrolysates. The most potent hydrolysate was obtained after 24 h incubation (ACE IC50 = 16.41 ± 6.06 μg/mL). Fourteen β-CN derived C-terminal Pro-containing di-, tri, and tetrapeptides which were predicted in silico to be released following An-PEP hydrolysis or which were detected by ultra-performance liquid chromatography-mass spectrometry (UPLC-MS/MS) in the 24 h hydrolysate were synthesised and characterised for their ACE inhibitory activity. The most potent inhibitory peptides were Ile-Gln-Ala (β-CN f187-189) and Val-Glu-Pro (β-CN f116-118) having ACE IC50 values of 32.9 ± 9.2 and 63.7 ± 12.0 μM, respectively. The hydrolysates generated appear to have the most potent ACE IC50 values reported for a food derived hydrolysate to date.

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